Separation of mixtures of complex biomolecules is an important element in high-throughput screening. The ability to sort biomolecules is particularly important in the fields of genomics, proteomics, and drug screening. In proteomics, for example, a vast diversity of (˜10,000 different species) protein and peptide samples need to be separated and analyzed. One goal of proteomics is to rapidly identify and quantitate all of the proteins expressed in a cell or a specific subset of proteins expressed in a cell that are associated with a particular pathway or disease. Similarly in genomics, the ability to analyze and separate a large number of genome fragments rapidly is highly desirable. One goal of genomics is to rapidly identify and quantitate all of the genomic modifications in a cell or any similarly small sample such as laser microcaptured biological samples. One goal of drug screening is to identify small molecules that bind to a cellular or extracellular protein which serves as the target for therapeutic intervention (e.g. a drug or other therapeutic treatment). Molecules that bind to a target protein (e.g. small organic molecules, peptides, or macromolecules such as proteins and aptamers) often modulate their activity. Such molecules themselves can serve as therapeutics or can guide the design of therapeutics. Current sorting techniques such as column purification, immunoprecipitation, or gel electrophoresis suffer from a number of profound drawbacks including low sensitivity, low speed and high cost.
Thus there remains a considerable need for alternative tools useful for robust high-throughput applications in genomics, proteomics, drug screening and aptamer selection.